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Database: UniProt
Entry: A0A090VFY0_9FLAO
LinkDB: A0A090VFY0_9FLAO
Original site: A0A090VFY0_9FLAO 
ID   A0A090VFY0_9FLAO        Unreviewed;      1007 AA.
AC   A0A090VFY0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JCM19300_2692 {ECO:0000313|EMBL:GAL63656.1};
OS   Algibacter lectus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Algibacter.
OX   NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL63656.1, ECO:0000313|Proteomes:UP000029644};
RN   [1] {ECO:0000313|EMBL:GAL63656.1, ECO:0000313|Proteomes:UP000029644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL63656.1,
RC   ECO:0000313|Proteomes:UP000029644};
RA   Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA   Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA   Sawabe T., Sawabe T.;
RT   "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT   SS8 and NR4.";
RL   Genome Announc. 2:e01168-14(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAL63656.1}.
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DR   EMBL; BBNQ01000013; GAL63656.1; -; Genomic_DNA.
DR   RefSeq; WP_042505472.1; NZ_BBNQ01000013.1.
DR   AlphaFoldDB; A0A090VFY0; -.
DR   OrthoDB; 1522078at2; -.
DR   Proteomes; UP000029644; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:GAL63656.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029644};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        419..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          473..702
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          751..866
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          898..997
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         799
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1007 AA;  116454 MW;  1728E142D27BABC1 CRC64;
     MNLANILVGT REGLFHFNQK TKAYVKIEND IKFIQTITRN YENTEFLIAD NRSIYKTNNY
     NSNDTKLDLI KIKSYKELIK DIVPINKNEL WVALWNGGID IINSNKAISE FKQNVIKKLE
     NHHTSTLLLA KNNKLWIGTR GEGLYCVDLL NETIKHYLPT LENGLTSNAI LSLHEDNLNN
     IWVGTRGGGL NMYEASLDKF NNFKENNAYR PKIVSAIEED YNGNIWMSTR NGITKFNIKT
     QRFIPFGVED GINENQFLFN SSTVNAQKKI IYFGCTDGFY SVFTTKLTPQ TILPTTVITS
     FAILGKTQEN KAMNSFKNIN EFYTYSGAPI ELPYNQNNIA VNFSSLDLTT PNKNQYAYKL
     KGLNNYWVYT SASNRNANYN DLSPGTYTFM VKSTNSDGAW NDTPAEVSFI INPPIWKSIW
     AIIAYVLLGI LIIYIGSILI RRWYLLKKNL VKETISREKD NELNRMKMIF FTDISHELRT
     PLSLILGTIE KVVKEKKFTL SPLTSQRIYN NTLRMHRLIN QIMDIRKFDE GKFKLKVSKN
     DIVKDINTIK NAFNDFAKIY EIDYDFTSNT KKTSGWYDVD LLEKILFNLV SNAFKYTAKN
     GKITVNLDVI KPNKNESEPH PFNGKYIRCS VRDNGLGIPK KDLEFIFDRY YQATKSQRNQ
     IPGTGIGMEL VHKLIERHHG TIKVESEENV YTEFTFCIPI SKDKYSKKER MQTSMPLKRN
     FIKNSEFQVI EEVSTEFNNK KNIEQKTKKS KVLVVEDNDD LRQMVKEELS DDFDIIEAPN
     GQEGYAQAMA EKPDLIISDI LMPIQDGLSM LKQIKKNAEF NNTPIFMLTA KNSDESKIEC
     LSLGANDYIE KPFSLEFLKW KVKNTFKTRH NLKEKYSKLI TTAPVDKHVD SNDEKFIKKL
     IKIIEDNMNN NLLSVEFLAS EIGMSRANLY RKVQQILNDT PVNFIKTIKL KRAAQLLKQD
     KMYISEVAYM TGFNNQKYFS KCFNKEYGMS PQSILNRIQN KIIFYKL
//
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